ArticleProceedings of the National Academy of Sciences of the United States of America2015
Secondary PDZ domain-binding site on class B plexins enhances the affinity for PDZ-RhoGEF.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Retinal ganglion cell-derived semaphorin 6A segregates starburst amacrine cell dendritic scaffolds to organize the mouse inner retina.Development (Cambridge, England) · 2024Article
- A balance of noncanonical Semaphorin signaling from the cerebrospinal fluid regulates apical cell dynamics during corticogenesis.Science advances · 2022Article
- Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.Chemical reviews · 2022Review
- Plexin-B2 controls the timing of differentiation and the motility of cerebellar granule neurons.eLife · 2021Article
- Architecture of the Sema3A/PlexinA4/Neuropilin tripartite complex.Nature communications · 2021Article
- Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95.The Journal of biological chemistry · 2020Article
- Article
- Regulation of the endosomal SNX27-retromer by OTULIN.Nature communications · 2019Article
- Structure function relations in PDZ-domain-containing proteins: Implications for protein networks in cellular signalling.Journal of biosciences · 2018Review
- Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex.eLife · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
PDZ domains are abundant protein interaction modules and typically recognize a short motif at the C terminus of their ligands, with a few residues in the motif endowing the binding specificity. The sequence-based rules, however, cannot fully account for the specificity between the vast number of PDZ domains and ligands in the cell. Plexins are transmembrane receptors that regulate processes such as axon guidance and angiogenesis. Two related guanine nucleotide exchange factors (GEFs), PDZ-RhoGEF and leukemia-associated RhoGEF (LARG), use their PDZ domains to bind class B plexins and play critical roles in signaling. Here, we present the crystal structure of the full-length cytoplasmic region of PlexinB2 in complex with the PDZ domain of PDZ-RhoGEF. The structure reveals that, in addition to the canonical C-terminal motif/PDZ interaction, the 3D domain of PlexinB2 forms a secondary interface with the PDZ domain. Our biophysical and cell-based assays show that the secondary interface contributes to the specific interaction between plexin and PDZ-RhoGEF and to signaling by plexin in the cell. Formation of secondary interfaces may be a general mechanism for increasing affinity and specificity of modular domain-mediated interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.